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Database: UniProt
Entry: A0A1X1Q671_9FIRM
LinkDB: A0A1X1Q671_9FIRM
Original site: A0A1X1Q671_9FIRM 
ID   A0A1X1Q671_9FIRM        Unreviewed;       482 AA.
AC   A0A1X1Q671;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Arginine decarboxylase {ECO:0000313|EMBL:ORU00225.1};
GN   ORFNames=D081_1319 {ECO:0000313|EMBL:ORU00225.1};
OS   Anaerovibrio sp. JC8.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Anaerovibrio.
OX   NCBI_TaxID=1240085 {ECO:0000313|EMBL:ORU00225.1, ECO:0000313|Proteomes:UP000192538};
RN   [1] {ECO:0000313|EMBL:ORU00225.1, ECO:0000313|Proteomes:UP000192538}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JC8 {ECO:0000313|EMBL:ORU00225.1,
RC   ECO:0000313|Proteomes:UP000192538};
RA   Evans P.N., Cheung J.L., Rosewarne C.P., Morrison M.;
RT   "Genomic and phenotypic data suggests Anaerovibrio species JC8 from the
RT   bovine rumen reduces fumarate and sulphite to decrease the inhibitory
RT   effect of hydrogen.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-I family.
CC       {ECO:0000256|ARBA:ARBA00010671}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ORU00225.1}.
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DR   EMBL; ANBM01000005; ORU00225.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X1Q671; -.
DR   STRING; 1240085.D081_1319; -.
DR   OrthoDB; 9815233at2; -.
DR   Proteomes; UP000192538; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   CDD; cd00615; Orn_deC_like; 1.
DR   Gene3D; 3.90.100.10; Orn/Lys/Arg decarboxylase, C-terminal domain; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR000310; Orn/Lys/Arg_deCO2ase_major_dom.
DR   InterPro; IPR008286; Prn/Lys/Arg_de-COase_C.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR43277; ARGININE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43277:SF4; ARGININE DECARBOXYLASE; 1.
DR   Pfam; PF01276; OKR_DC_1; 1.
DR   Pfam; PF03711; OKR_DC_1_C; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00703; OKR_DC_1; 1.
PE   3: Inferred from homology;
FT   DOMAIN          223..237
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS00703"
SQ   SEQUENCE   482 AA;  53005 MW;  13D18DFBF11C36C6 CRC64;
     MKYYSQDSAP ILEALEKMKR ARLVPFDVPG HKRGRGNPEL TEFLGEQCLS VDVNSMKMLD
     NLCHPVSVIK DAEQLAADAF GAAHAFFMVG GTTSAVQAMV MTACKRGDKI IIPRNVHRSA
     INAMILCGAV PVYVNPQMDS MLGISLGMSV SDVEQAIREN PDAKAVFVNN PTYYGICSDI
     KSIAKLAHDN GMLLLADEAH GSHLYFSDKL PVAAMHAGAD MAALSMHKSG GSLTQSSMLL
     IGDSVPEGYV HQIINLTQTT SASYLLLASL DVSRRNMALR GGEMIDKIID LVEYARDEIN
     AIGDYYAYSK ELINGDSIFD FDITKLSVYT RSIGLAGIEV YDLLRDEYDI QTEFGDIANL
     LAYVSVGDRL KDIERLVSAL AEIRRNYRQT GRKMLKAEYI NPQVVCGPQE AFYGAKESLP
     IGDTVGRVCS EFVMCYPPGI PILAPGERIT EEILQYIRYA KKKGCSMTGP EDMDIRFLNV
     MK
//
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